1k8b: Difference between revisions
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'''NMR Structure Analysis of the N-terminal Domain of Archaeal Translation Initiation Factor 2 Subunit beta'''<br /> | '''NMR Structure Analysis of the N-terminal Domain of Archaeal Translation Initiation Factor 2 Subunit beta'''<br /> | ||
==Overview== | ==Overview== | ||
The beta subunit of archaeal translation initiation factor 2 (aIF2beta) is | The beta subunit of archaeal translation initiation factor 2 (aIF2beta) is a representative of a family of proteins whose members include the beta subunit of eukaryotic translation initiation factor 2 (eIF2beta) and the N-terminal domain within translation initiation factor 5 (eIF5); no members of this family of proteins have been structurally characterized up to this time. In the work presented here, aIF2beta from Methanococcus jannaschii was expressed in Escherichia coli, purified, and analyzed using multidimensional NMR methods. The aIF2beta was found to contain two independent structural domains. The N-terminal domain contains a four-stranded antiparallel beta sheet and two alpha helices, and is structurally similar to the DNA-binding domain of a yeast heat shock transcription factor and a domain within ribosomal protein S4. This structural similarity was an unanticipated result, since no significant homology was detected at the level of primary sequence. The C-terminal domain of aIF2beta contains a zinc-binding motif of three antiparallel beta strands, with four conserved cysteines arranged as two CXXC units separated by 17 residues. Conserved residues on the surface of each domain that are likely candidates for direct interaction with other components of the translational apparatus were identified. The significant primary sequence homology between archaeal aIF2beta and the eukaryotic eIF2beta and eIF5, when combined with the structural results in the work presented here, permitted structural features to be predicted for these latter two eukaryotic proteins. | ||
==About this Structure== | ==About this Structure== | ||
1K8B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http:// | 1K8B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K8B OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cho, S.]] | [[Category: Cho, S.]] | ||
[[Category: Hoffman, D | [[Category: Hoffman, D W.]] | ||
[[Category: aif2 subunit beta]] | [[Category: aif2 subunit beta]] | ||
[[Category: n-terminal domain]] | [[Category: n-terminal domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:15 2008'' | ||
Revision as of 14:31, 21 February 2008
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NMR Structure Analysis of the N-terminal Domain of Archaeal Translation Initiation Factor 2 Subunit beta
OverviewOverview
The beta subunit of archaeal translation initiation factor 2 (aIF2beta) is a representative of a family of proteins whose members include the beta subunit of eukaryotic translation initiation factor 2 (eIF2beta) and the N-terminal domain within translation initiation factor 5 (eIF5); no members of this family of proteins have been structurally characterized up to this time. In the work presented here, aIF2beta from Methanococcus jannaschii was expressed in Escherichia coli, purified, and analyzed using multidimensional NMR methods. The aIF2beta was found to contain two independent structural domains. The N-terminal domain contains a four-stranded antiparallel beta sheet and two alpha helices, and is structurally similar to the DNA-binding domain of a yeast heat shock transcription factor and a domain within ribosomal protein S4. This structural similarity was an unanticipated result, since no significant homology was detected at the level of primary sequence. The C-terminal domain of aIF2beta contains a zinc-binding motif of three antiparallel beta strands, with four conserved cysteines arranged as two CXXC units separated by 17 residues. Conserved residues on the surface of each domain that are likely candidates for direct interaction with other components of the translational apparatus were identified. The significant primary sequence homology between archaeal aIF2beta and the eukaryotic eIF2beta and eIF5, when combined with the structural results in the work presented here, permitted structural features to be predicted for these latter two eukaryotic proteins.
About this StructureAbout this Structure
1K8B is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the beta subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: a representative of the eIF2beta/eIF5 family of proteins., Cho S, Hoffman DW, Biochemistry. 2002 May 7;41(18):5730-42. PMID:11980477
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